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1

Tanaka, Nao, and Toyonobu Usuki. "Preparation of Protected 13Cn-Labeled Isodesmosines: Mechanistic Insight of Isodesmosine Formation." Natural Product Communications 14, no. 6 (June 2019): 1934578X1984996. http://dx.doi.org/10.1177/1934578x19849967.

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2

Baut, Daria A., Nao Tanaka, Reiko Yokoo, and Toyonobu Usuki. "Preparation of isodesmosine‐KLH conjugate for ELISA system." Chirality 32, no. 4 (February 6, 2020): 431–36. http://dx.doi.org/10.1002/chir.23175.

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3

Giummelly, Philippe, Bernard Botton, Raphaëlle Friot, Deddi Prima-Putra, and Jeffrey Atkinson. "Measurement of desmosine and isodesmosine by capillary zone electrophoresis." Journal of Chromatography A 710, no. 2 (September 1995): 357–60. http://dx.doi.org/10.1016/0021-9673(95)00487-4.

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4

AIKAWA, JUNICHIRO, HIROSHI MUNAKATA, MAMORU ISEMURA, and ZENSAKU YOSIZAWA. "Sulfated glycopeptides, containing desmosine and isodesmosine, isolated from porcine aorta." Tohoku Journal of Experimental Medicine 145, no. 2 (1985): 175–83. http://dx.doi.org/10.1620/tjem.145.175.

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5

Sampedro, Inmaculada, Junichi Kato, and Jane E. Hill. "Elastin degradation product isodesmosine is a chemoattractant for Pseudomonas aeruginosa." Microbiology 161, no. 7 (July 1, 2015): 1496–503. http://dx.doi.org/10.1099/mic.0.000090.

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6

Ma, Shuren, Yong Y. Lin, and Gerard M. Turino. "Measurements of Desmosine and Isodesmosine by Mass Spectrometry in COPD." Chest 131, no. 5 (May 2007): 1363–71. http://dx.doi.org/10.1378/chest.06-2251.

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7

Cumiskey, Wayne R., Edward D. Pagani, and Donald C. Bode. "Enrichment and analysis of desmosine and isodesmosine in biological fluids." Journal of Chromatography B: Biomedical Sciences and Applications 668, no. 2 (June 1995): 199–207. http://dx.doi.org/10.1016/0378-4347(95)00092-w.

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8

Tan, C. I., G. N. Kent, A. G. Randall, S. J. Edmondston, and K. P. Singer. "COLLAGEN AND ELASTIN CROSSLINKS IN HUMAN INTERVERTEBRAL DISCS AND LIGAMENTUM FLAVUM: AGE, GENDER AND SPINAL LEVEL INFLUENCES." Journal of Musculoskeletal Research 06, no. 02 (June 2002): 73–88. http://dx.doi.org/10.1142/s021895770200068x.

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The collagen and elastin content and extent of collagen crosslinks were determined in human formalin-fixed and unfixed intervertebral discs and ligamentum flava. Tissue samples from cadaveric spinal discs (n = 77) and ligamentum flava (n = 364) were obtained from 24 formalin-fixed and 2 fresh spines. The mean age of all cases was 57±26 years. Spinal ligament and disc samples were harvested and analyzed for collagen, and crosslinks of pyridinoline, deoxypyridinoline, and elastin crosslinks isodesmosine and desmosine. Collagen and elastin crosslinks were extracted from hydrolyzed samples by cellulose partition chromatography, and analyzed by reverse-phase HPLC. Elastin crosslinks were only detected in 4 lumbar discs (mean 0.04±0.01 nmol/mg dry wt) but yielded results for all ligamentum flavum samples (mean 20.2±6.4 nmol/mg dry wt). For ligamentum flavum, the collagen and collagen crosslinks increased significantly with age (p < 0.05), whereas elastin content decreased significantly with age but only for the lumbar region (p < 0.05). Collagen and elastin content were significantly higher in females (p < 0.01) and collagen, pyridinoline and isodesmosine were significantly higher in the lumbar region (p < 0.01). Elastin detected in lumbar discs was significantly less than that found in ligamentum flavum. The collagen and elastin content and extent of collagen crosslinks in ligamentum matrix varied significantly depending on the age, gender and spinal region.
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9

Boutin, Michel, Carl Berthelette, François G. Gervais, Mary-Beth Scholand, John Hoidal, Mark F. Leppert, Kevin P. Bateman, and Pierre Thibault. "High-Sensitivity NanoLC−MS/MS Analysis of Urinary Desmosine and Isodesmosine." Analytical Chemistry 81, no. 5 (March 2009): 1881–87. http://dx.doi.org/10.1021/ac801745d.

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10

Minkin, Ruth, Gagangeet Sandhu, Horiana Grosu, Lori Tartell, Shuren Ma, Yong Y. Lin, Edward Eden, and Gerard M. Turino. "Desmosine and Isodesmosine as a Novel Biomarker for Pulmonary Arterial Hypertension." American Journal of Therapeutics 24, no. 4 (2017): e399-e404. http://dx.doi.org/10.1097/mjt.0000000000000260.

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11

Tanaka, Nao, Manami Kurita, Yuko Murakami, and Toyonobu Usuki. "Chichibabin and IsoChichibabin Pyridinium Syntheses of Isodesmosine, Desmosine, and their Derivatives." European Journal of Organic Chemistry 2018, no. 43 (October 24, 2018): 6002–9. http://dx.doi.org/10.1002/ejoc.201801156.

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12

Sugimura, Takanori, Akira Komatsu, Yohei Koseki, and Toyonobu Usuki. "Pr(OTf)3-promoted Chichibabin pyridine synthesis of isodesmosine in H2O/MeOH." Tetrahedron Letters 55, no. 46 (November 2014): 6343–46. http://dx.doi.org/10.1016/j.tetlet.2014.09.097.

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13

Rathod, Pratikkumar, Manjeet Kaur, Hsin-Pin Ho, Marissa E. Louis, Basant Dhital, Philip Durlik, Gregory S. Boutis, Kevin J. Mark, Jong I. Lee, and Emmanuel J. Chang. "Quantification of desmosine and isodesmosine using MALDI-ion trap tandem mass spectrometry." Analytical and Bioanalytical Chemistry 410, no. 26 (July 31, 2018): 6881–89. http://dx.doi.org/10.1007/s00216-018-1288-z.

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14

Salomoni, M., M. Muda, E. Zuccato, and E. Mussini. "High-performance liquid chromatographic determination of desmosine and isodesmosine after phenylisothiocyanate derivatization." Journal of Chromatography B: Biomedical Sciences and Applications 572, no. 1-2 (December 1991): 312–16. http://dx.doi.org/10.1016/0378-4347(91)80496-y.

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15

Mižíková, Ivana, Jordi Ruiz-Camp, Heiko Steenbock, Alicia Madurga, István Vadász, Susanne Herold, Konstantin Mayer, Werner Seeger, Jürgen Brinckmann, and Rory E. Morty. "Collagen and elastin cross-linking is altered during aberrant late lung development associated with hyperoxia." American Journal of Physiology-Lung Cellular and Molecular Physiology 308, no. 11 (June 1, 2015): L1145—L1158. http://dx.doi.org/10.1152/ajplung.00039.2015.

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Maturation of the lung extracellular matrix (ECM) plays an important role in the formation of alveolar gas exchange units. A key step in ECM maturation is cross-linking of collagen and elastin, which imparts stability and functionality to the ECM. During aberrant late lung development in bronchopulmonary dysplasia (BPD) patients and animal models of BPD, alveolarization is blocked, and the function of ECM cross-linking enzymes is deregulated, suggesting that perturbed ECM cross-linking may impact alveolarization. In a hyperoxia (85% O2)-based mouse model of BPD, blunted alveolarization was accompanied by alterations to lung collagen and elastin levels and cross-linking. Total collagen levels were increased (by 63%). The abundance of dihydroxylysinonorleucine collagen cross-links and the dihydroxylysinonorleucine-to-hydroxylysinonorleucine ratio were increased by 11 and 18%, respectively, suggestive of a profibrotic state. In contrast, insoluble elastin levels and the abundance of the elastin cross-links desmosine and isodesmosine in insoluble elastin were decreased by 35, 30, and 21%, respectively. The lung collagen-to-elastin ratio was threefold increased. Treatment of hyperoxia-exposed newborn mice with the lysyl oxidase inhibitor β-aminopropionitrile partially restored normal collagen levels, normalized the dihydroxylysinonorleucine-to-hydroxylysinonorleucine ratio, partially normalized desmosine and isodesmosine cross-links in insoluble elastin, and partially restored elastin foci structure in the developing septa. However, β-aminopropionitrile administration concomitant with hyperoxia exposure did not improve alveolarization, evident from unchanged alveolar surface area and alveoli number, and worsened septal thickening (increased by 12%). These data demonstrate that collagen and elastin cross-linking are perturbed during the arrested alveolarization of developing mouse lungs exposed to hyperoxia.
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16

Ongay, Sara, Marijke Sikma, Peter Horvatovich, Jos Hermans, Bruce E. Miller, Nick H. T. ten Hacken, and Rainer Bischoff. "Free Urinary Desmosine and Isodesmosine as COPD Biomarkers: The Relevance of Confounding Factors." Chronic Obstructive Pulmonary Diseases: Journal of the COPD Foundation 3, no. 2 (2016): 560–69. http://dx.doi.org/10.15326/jcopdf.3.2.2015.0159.

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17

Viglio, S., P. Iadarola, A. Lupi, R. Trisolini, C. Tinelli, B. Balbi, V. Grassi, et al. "MEKC of desmosine and isodesmosine in urine of chronic destructive lung disease patients." European Respiratory Journal 15, no. 6 (June 2000): 1039. http://dx.doi.org/10.1034/j.1399-3003.2000.01511.x.

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18

Koseki, Yohei, Takanori Sugimura, Keita Ogawa, Rina Suzuki, Haruka Yamada, Noriyuki Suzuki, Yoshiro Masuyama, Yong Y. Lin, and Toyonobu Usuki. "Total Synthesis of Isodesmosine by Stepwise, Regioselective Negishi and Sonogashira Cross-Coupling Reactions." European Journal of Organic Chemistry 2015, no. 18 (May 15, 2015): 4024–32. http://dx.doi.org/10.1002/ejoc.201500449.

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19

Ongay, Sara, Jos Hermans, Andries P. Bruins, Adrianus M. C. H. Nieuwendijk, Hermen Overkleeft, and Rainer Bischoff. "Electron Transfer and Collision Induced Dissociation of Non-Derivatized and Derivatized Desmosine and Isodesmosine." Journal of The American Society for Mass Spectrometry 24, no. 1 (November 27, 2012): 83–91. http://dx.doi.org/10.1007/s13361-012-0504-x.

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20

Umeda, Hideyuki, Masanori Aikawa, and Peter Libby. "Liberation of desmosine and isodesmosine as amino acids from insoluble elastin by elastolytic proteases." Biochemical and Biophysical Research Communications 411, no. 2 (July 2011): 281–86. http://dx.doi.org/10.1016/j.bbrc.2011.06.124.

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21

Fregonese, Laura, Fabio Ferrari, Marco Fumagalli, Maurizio Luisetti, Jan Stolk, and Paolo Iadarola. "Long-term Variability of Desmosine/Isodesmosine as Biomarker in Alpha-1-antritrypsin Deficiency–related COPD." COPD: Journal of Chronic Obstructive Pulmonary Disease 8, no. 5 (July 27, 2011): 329–33. http://dx.doi.org/10.3109/15412555.2011.589871.

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22

Albarbarawi, Osama, Alun Barton, ZhaoSheng Lin, Eddie Takahashi, Ajay Buddharaju, Jeffrey Brady, Douglas Miller, Colin N. A. Palmer, and Jeffrey T. J. Huang. "Measurement of Urinary Total Desmosine and Isodesmosine Using Isotope-Dilution Liquid Chromatography-Tandem Mass Spectrometry." Analytical Chemistry 82, no. 9 (May 2010): 3745–50. http://dx.doi.org/10.1021/ac100152f.

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23

Usuki, Toyonobu, Takanori Sugimura, Akira Komatsu, and Yohei Koseki. "Biomimetic Chichibabin Pyridine Synthesis of the COPD Biomarkers and Elastin Cross-Linkers Isodesmosine and Desmosine." Organic Letters 16, no. 6 (March 5, 2014): 1672–75. http://dx.doi.org/10.1021/ol500333t.

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24

Liu, Xingjian, Shuren Ma, Sophie Liu, Ming Liu, Gerard Turino, and Jerome Cantor. "The Ratio of Free to Bound Desmosine and Isodesmosine May Reflect Emphysematous Changes in COPD." Lung 193, no. 3 (March 12, 2015): 329–34. http://dx.doi.org/10.1007/s00408-015-9712-z.

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25

Soskel, Norman T. "High-performance liquid chromatographic quantitation of desmosine plus isodesmosine in elastin and whole tissue hydrolysates." Analytical Biochemistry 160, no. 1 (January 1987): 98–104. http://dx.doi.org/10.1016/0003-2697(87)90618-x.

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26

Tyagi, Suresh C., and Sanford R. Simon. "Elastin-derived peptide binding to a hydrophobic domain on neutrophil elastase." Biochemistry and Cell Biology 72, no. 9-10 (September 1, 1994): 419–27. http://dx.doi.org/10.1139/o94-056.

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To understand the contributions of binding of elastin to domains removed from the active site of neutrophil elastase, we isolated an elastin-derived peptide (EDP) fraction, which we have previously shown was tightly linked to neutrophil elastase after prolonged digestion of elastin but which can be released from the enzyme with hydroxylamine. Elastin from human aorta was incubated with human neutrophil elastase under conditions favoring proteolysis. Low molecular weight species, including free EDP, were separated from the protein fraction by a small centrifuged gel filtration column. The high molecular weight protein fraction was subjected directly to 0.5 M hydroxylamine. The reaction mixture was then fractionated on a phosphocellulose column using an ionic gradient. A fraction was collected that exhibited fluorescence with a peak at ~410 nm when excited at 320 nm, indicating the presence of desmosine and (or) isodesmosine. A second peak with amidolytic activity towards methoxysuccinyl-Ala-Ala-Pro-Val-p-nitroaniline (MeOSucAAPVpNa), but no fluorescence at 410 nm was also detected at the same elution volume where free elastase appeared. After removal of low molecular weight digestion products but prior to treatment with hydroxylamine, the putative elastase–EDP complex possessed no amidolytic activity towards MeOSucAAPVpNa. When the liberated EDP was added to elastase in an amidolytic assay, the EDP behaved as only a partial noncompetitive inhibitor [Formula: see text], but bound with high affinity to neutrophil elastase [Formula: see text], as detected by its ability to quench elastase endogenous fluorescence. The complete emission spectrum of the mixture of elastase and EDP obtained at excitation wavelengths specific for tryptophan and desmosine/isodesmosine suggests that the EDP was in a hydrophobic environment which was close to at least one of the three tryptophan residues in the enzyme. Based on fluorescence energy transfer, we have estimated a distance between the elastase and EDP of ~10 ± 3 Å (1 Å = 0.1 nm) during elastinolysis. This pattern of binding to a hydrophobic site on neutrophil elastase without competitive inhibition of amidolytic activity was consistent with the importance of hydrophobic interactions between neutrophil elastase and elastin within a region of the enzyme removed from the active site.Key words: proteinase, elastase, elastin, extracellular matrix, elastin-derived peptide.
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27

Ma, Shuren, Patrick Geraghty, Abdoulaye Dabo, Cormac McCarthy, N. Gerry McElvaney, and Gerard M. Turino. "Cystic fibrosis disease severity correlates with plasma levels of desmosine and isodesmosine, biomarkers of elastin degradation." ERJ Open Research 5, no. 2 (April 2019): 00250–2018. http://dx.doi.org/10.1183/23120541.00250-2018.

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28

Osakabe, Toru, Yoshiyuki Seyama, and Saburo Yamashita. "Comparison of elisa and hplc for the determination of desmosine or isodesmosine in aortic tissue elastin." Journal of Clinical Laboratory Analysis 9, no. 5 (1995): 293–96. http://dx.doi.org/10.1002/jcla.1860090503.

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29

Tan, Celia I. C., Sonia Dunn, G. Neil Kent, Andrew G. Randall, Stephen J. Edmondston, and Kevin P. Singer. "DOES FORMALIN-FIXATION ALTER THE EXTENT OF COLLAGEN AND ELASTIN CROSSLINKS IN HUMAN SPINAL INTERVERTEBRAL DISCS AND LIGAMENTUM FLAVA?" Journal of Musculoskeletal Research 06, no. 02 (June 2002): 89–99. http://dx.doi.org/10.1142/s0218957702000691.

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The effect of formalin-fixation on the extent of collagen and elastin crosslinks in the matrix of human spinal intervertebral discs and ligamentum flava tissues was evaluated. Fresh discs (n = 5) and ligamentum flava (n = 22) were harvested and separated into two samples. One sample was stored in 10% buffered formalin and the other control sample in a freezer at -20°C. Using HPLC the paired anular (n = 72), nuclear (n = 22) and liagmentum flavum (n = 58) samples were dried, hydrolyzed and assayed for collagen and elastin crosslinks over a 25-week period. There were no significant differences in the collagen, isodesmosine and desmosine content, and the extent of pyridinoline and deoxypyridinoline crosslinks, between fresh and formalin-fixed disc and ligament samples after 25 weeks of formalin fixation. Short-term formalin-fixation does not significantly influence the collagen and elastin crosslink content or the extent of insoluble collagen crosslinks in spinal disc and ligamentum flavum tissues.
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30

Usuki, Toyonobu, Takanori Sugimura, Akira Komatsu, and Yohei Koseki. "ChemInform Abstract: Biomimetic Chichibabin Pyridine Synthesis of the COPD Biomarkers and Elastin Cross-Linkers Isodesmosine and Desmosine." ChemInform 45, no. 36 (August 21, 2014): no. http://dx.doi.org/10.1002/chin.201436200.

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31

Shiraishi, Kohei, Kazue Matsuzaki, Akinori Matsumoto, Yuuki Hashimoto, and Kazuhiko Iba. "Development of a Robust LC-MS/MS Method for Determination of Desmosine and Isodesmosine in Human Urine." Journal of Oleo Science 59, no. 8 (2010): 431–39. http://dx.doi.org/10.5650/jos.59.431.

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32

Tanigawa, Takahiro, Akira Komatsu, and Toyonobu Usuki. "[13C3,15N1]-labeled isodesmosine: A potential internal standard for LC–MS/MS analysis of desmosines in elastin degradation." Bioorganic & Medicinal Chemistry Letters 25, no. 10 (May 2015): 2046–49. http://dx.doi.org/10.1016/j.bmcl.2015.03.084.

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33

Tobias, JW, MM Bern, PA Netland, and BR Zetter. "Monocyte adhesion to subendothelial components." Blood 69, no. 4 (April 1, 1987): 1265–68. http://dx.doi.org/10.1182/blood.v69.4.1265.1265.

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Abstract Human monocytes have been shown to penetrate the endothelial layer of large blood vessels and to adhere to the subendothelial basement membrane. To determine the active components of this process, we have studied the ability of monocytes to adhere to isolated components of the subendothelial matrix. Using a quantitative dot-blot adhesion assay, we find that monocytes adhere preferentially to immobilized laminin and elastin. The monocytes adhere less well to fibronectin and bind poorly or not at all to collagen types I and IV, or to heparan sulfate. Monocyte binding to elastin requires an intact, crosslinked molecule as no binding was observed to soluble, acid-alcohol elastin extracts, to pepsin or elastase digests of elastin, to tropoelastin monomer, or to desmosine/isodesmosine crosslinks. Similar binding profiles to elastin, laminin, and fibronectin were seen with the established human leukocyte cell line U937. The promyelocytic cell line HL60 adhered equally well to laminin but showed slightly reduced adhesion to elastin when compared with the fresh monocytes or U937 cells. Freshly isolated human erythrocytes did not demonstrate significant adhesion to fibronectin, laminin, or elastin.
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34

Tobias, JW, MM Bern, PA Netland, and BR Zetter. "Monocyte adhesion to subendothelial components." Blood 69, no. 4 (April 1, 1987): 1265–68. http://dx.doi.org/10.1182/blood.v69.4.1265.bloodjournal6941265.

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Human monocytes have been shown to penetrate the endothelial layer of large blood vessels and to adhere to the subendothelial basement membrane. To determine the active components of this process, we have studied the ability of monocytes to adhere to isolated components of the subendothelial matrix. Using a quantitative dot-blot adhesion assay, we find that monocytes adhere preferentially to immobilized laminin and elastin. The monocytes adhere less well to fibronectin and bind poorly or not at all to collagen types I and IV, or to heparan sulfate. Monocyte binding to elastin requires an intact, crosslinked molecule as no binding was observed to soluble, acid-alcohol elastin extracts, to pepsin or elastase digests of elastin, to tropoelastin monomer, or to desmosine/isodesmosine crosslinks. Similar binding profiles to elastin, laminin, and fibronectin were seen with the established human leukocyte cell line U937. The promyelocytic cell line HL60 adhered equally well to laminin but showed slightly reduced adhesion to elastin when compared with the fresh monocytes or U937 cells. Freshly isolated human erythrocytes did not demonstrate significant adhesion to fibronectin, laminin, or elastin.
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35

Zarkadas, Constantinos G., George C. Zarkadas, Constantinos N. Karatzas, Ali D. Khalili, and Quang Nguyen. "Rapid method for determining desmosine, isodesmosine, 5-hydroxylysine, tryptophan, lysinoalanine and the amino sugars in proteins and tissues." Journal of Chromatography B: Biomedical Sciences and Applications 378 (January 1986): 67–76. http://dx.doi.org/10.1016/s0378-4347(00)80700-8.

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36

KIKUCHI, Yasuo, Osamu TSUCHIKURA, Masahiro HIRAMA, and Nobuo TAMIYA. "Desmosine and isodesmosine as cross-links in the hinge-ligament protein of bivalves. 3,3'-Methylenebistyrosine as an artefact." European Journal of Biochemistry 164, no. 2 (April 1987): 397–402. http://dx.doi.org/10.1111/j.1432-1033.1987.tb11071.x.

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37

Charpiot, P., R. Calaf, C. Chareyre, P. H. Rolland, and D. Gar�on. "Rapid determination of desmosine and isodesmosine in tissue hydrolysates by isocratic high performance liquid chromatography and precolumn derivatization." Amino Acids 6, no. 1 (1994): 57–63. http://dx.doi.org/10.1007/bf00808123.

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38

Getie, Melkamu, Klaus Raith, and Reinhard H. H. Neubert. "LC/ESI-MS analysis of two elastin cross-links, desmosine and isodesmosine, and their radiation-induced degradation products." Biochimica et Biophysica Acta (BBA) - General Subjects 1624, no. 1-3 (December 2003): 81–87. http://dx.doi.org/10.1016/j.bbagen.2003.09.013.

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39

Viglio, Simona, Giuseppe Zanaboni, Maurizio Luisetti, Rocco Trisolini, Rudi Grimm, Giuseppe Cetta, and Paolo Iadarola. "Micellar electrokinetic chromatography for the determination of urinary desmosine and isodesmosine in patients affected by chronic obstructive pulmonary disease." Journal of Chromatography B: Biomedical Sciences and Applications 714, no. 1 (August 1998): 87–98. http://dx.doi.org/10.1016/s0378-4347(98)00046-2.

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40

Ma, S., S. Lieberman, G. M. Turino, and Y. Y. Lin. "The detection and quantitation of free desmosine and isodesmosine in human urine and their peptide-bound forms in sputum." Proceedings of the National Academy of Sciences 100, no. 22 (October 16, 2003): 12941–43. http://dx.doi.org/10.1073/pnas.2235344100.

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41

Ma, Shuren, Gerard M. Turino, and Yong Y. Lin. "Quantitation of desmosine and isodesmosine in urine, plasma, and sputum by LC–MS/MS as biomarkers for elastin degradation." Journal of Chromatography B 879, no. 21 (July 2011): 1893–98. http://dx.doi.org/10.1016/j.jchromb.2011.05.011.

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42

Lunte, Susan M., Tariq Mohabbat, Osborne S. Wong, and Theodore Kuwana. "Determination of desmosine, isodesmosine, and other amino acids by liquid chromatography with electrochemical detection following precolumn derivatization with naphthalenedialdehyde/cyanide." Analytical Biochemistry 178, no. 1 (April 1989): 202–7. http://dx.doi.org/10.1016/0003-2697(89)90380-1.

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43

Devenport, Neil A., James C. Reynolds, Ved Parkash, Jason Cook, Daniel J. Weston, and Colin S. Creaser. "Determination of free desmosine and isodesmosine as urinary biomarkers of lung disorder using ultra performance liquid chromatography–ion mobility-mass spectrometry." Journal of Chromatography B 879, no. 32 (December 2011): 3797–801. http://dx.doi.org/10.1016/j.jchromb.2011.10.016.

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44

Huang, Jing, and Jingwu Kang. "Separation and measurement of desmosine and isodesmosine in vascular tissue hydrolysates by micellar electrokinetic capillary chromatography with a mixed micelle system." Journal of Chromatography A 1175, no. 2 (December 2007): 294–96. http://dx.doi.org/10.1016/j.chroma.2007.10.091.

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45

Viglio, Simona, Laura Annovazzi, Maurizio Luisetti, Jan Stolk, Begoña Casado, and Paolo Iadarola. "Progress in the methodological strategies for the detection in real samples of desmosine and isodesmosine, two biological markers of elastin degradation." Journal of Separation Science 30, no. 2 (February 2007): 202–13. http://dx.doi.org/10.1002/jssc.200600260.

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46

Oleggini, Roberta, and Armando Di Donato. "Lysyl oxidase regulates MMTV promoter: indirect evidence of histone H1 involvement." Biochemistry and Cell Biology 89, no. 6 (December 2011): 522–32. http://dx.doi.org/10.1139/o11-049.

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Lysyl oxidase (LOX) is the enzyme that facilitates the cross-linking of collagen and elastin, although other functions for this enzyme have been indicated. Of these other functions, we describe herein the ability of LOX to regulate several gene promoters, like collagen III, elastin, and cyclin D1. We have previously demonstrated a specific binding between LOX and histone H1, in vitro. Therefore, we investigated whether LOX would affect the mouse mammary tumor virus (MMTV) promoter and its glucocorticoid regulation, which depends on the phophorylation status of histone H1. Our results show that the over-expression of recombinant human LOX was able to trigger MMTV activity, both in the presence and absence of glucocorticoids. Moreover, we demonstrated that histone H1 from cells expressing recombinant LOX contained isodesmosine and desmosine, indicating specific lysyl-oxidase-dependent lysine modifications. Finally, we were able to co-immunoprecipitate the exogenous LOX and histone H1 from the LOX transfected cells. The data are compatible with a decreased positive charge of histone H1, owing to deamination by LOX of its lysine residues. This event would favor H1 detachment from the target DNA, and consequent opening of the MMTV promoter structure to the activating transcription factors. The presented data, therefore, suggest a possible histone-H1-dependent mechanism for the modulation of MMTV promoter by LOX.
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47

Albarbarawi, Osama, Alun Barton, Douglas Miller, Charles McSharry, Rekha Chaudhuri, Neil C. Thomson, Colin NA Palmer, Graham Devereux, and Jeffrey T.-J. Huang. "Characterization and validation of an isotope-dilution LC–MS/MS method for quantification of total desmosine and isodesmosine in plasma and serum." Bioanalysis 5, no. 16 (August 2013): 1991–2001. http://dx.doi.org/10.4155/bio.13.164.

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48

Kaga, Naoko, Sanae Soma, Tsutomu Fujimura, Kuniaki Seyama, Yoshinosuke Fukuchi, and Kimie Murayama. "Quantification of elastin cross-linking amino acids, desmosine and isodesmosine, in hydrolysates of rat lung by ion-pair liquid chromatography–mass spectrometry." Analytical Biochemistry 318, no. 1 (July 2003): 25–29. http://dx.doi.org/10.1016/s0003-2697(03)00134-9.

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49

Yamaguchi, Yu, Jun Haginaka, Masaru Kunitomo, Hiroyuki Yasuda, and Yoshio Bandô. "High-performance liquid chromatographic determination of desmosine and isodesmosine in tissues and its application to studies of alteration of elastin induced by atherosclerosis." Journal of Chromatography B: Biomedical Sciences and Applications 422 (January 1987): 53–59. http://dx.doi.org/10.1016/0378-4347(87)80439-5.

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50

Ongay, Sara, Gert Hendriks, Jos Hermans, Maarten van den Berge, Nick H. T. ten Hacken, Nico C. van de Merbel, and Rainer Bischoff. "Quantification of free and total desmosine and isodesmosine in human urine by liquid chromatography tandem mass spectrometry: A comparison of the surrogate-analyte and the surrogate-matrix approach for quantitation." Journal of Chromatography A 1326 (January 2014): 13–19. http://dx.doi.org/10.1016/j.chroma.2013.12.035.

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